ID   H6PWF3_RICP3            Unreviewed;       928 AA.
AC   H6PWF3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:AFB25856.1};
GN   OrderedLocusNames=RSA_01250 {ECO:0000313|EMBL:AFB25856.1};
OS   Rickettsia philipii (strain 364D).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=481009 {ECO:0000313|EMBL:AFB25856.1, ECO:0000313|Proteomes:UP000007997};
RN   [1] {ECO:0000313|Proteomes:UP000007997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=364D {ECO:0000313|Proteomes:UP000007997};
RA   Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT   "Complete genome sequence of Rickettsia philipii strain 364D.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP003308; AFB25856.1; -; Genomic_DNA.
DR   RefSeq; WP_014364441.1; NC_016930.1.
DR   AlphaFoldDB; H6PWF3; -.
DR   KEGG; rph:RSA_01250; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000007997; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AFB25856.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          585..778
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   928 AA;  104010 MW;  2269AA3E7628C699 CRC64;
     MEEDFKKTGY LFGGNAVFVE ELYKQYLANP ASVDQTWQEF FAGIQDNNTL LNKSTAKIII
     PDEIKKESLN NNLSSEDLNS LKAKEMINAY RKHAHYLANL DPLGLELRKT KNDLKLNIET
     FGLDSSQLEE NINITDEFVG TWNCKLSELV TKFDKVYTGS IGVEFEQIEN VARKNWLYNK
     LESEVTFSSE DKKTILNDLV EVEGFEQYLH TKFPGTKRFS IEGGDASIVA MSKAIDLSMH
     HGVSEIVIGM AHRGRLNTLT KVVGKPYKAV IAGFISGSVF PDELNVSGDV KYHLGYSFDR
     TLEDKKIHLS LADNPSHLEA VNPIVAGKVR AKQDMLGDTK RSKVKAILVH GDAAFCGQGV
     VAESLSMSPL AAYDIGGILH FVINNQLGFT ANAADTRASR YSTEFAKIIA APILHVNGDD
     IEAVLKATNI AVEYRQKFGK DVVVEIICYR KYGHNEGDEP MYTQGKMYNI IKNKLTPGNI
     YANELVKSGV IDNNYFAKLK EEFKAKLDKE YEQAKSYKQE AHCLGGLWQG ISRIRTQATI
     TGISKKTLHD LGTKLCEIPK DFAVNPKLVK LFEARKATLT ADQPIDWATA EQLAFASLLA
     SGTNIRLTGQ DSGRGTFSHR HSVLHNQIDG TTYIPLNNLS KEQAKYEVAD SHLSEYAVLG
     FEYGYSLANP NNLVLWEAQF GDFANGAQII FDQFISSSET KWLRMSGLVV LLPHAFEGQG
     PEHSSARLER FLQLAAENNM YVTYPTTPAS IFHLLRRQIL DDTRKPLIVM SPKSLLRHKY
     AVSKLDELGE NTTFLPVLDE VTKVDTNNIT KVILCSGKVY YDLFEMRGNN SNIAIIRLEQ
     LYPFEKKLVA SLLKKYNRTQ EFIWCQEEPK NMGTWCYIVS HLNDALKEAG IKNEFKYVGR
     EESASPAVGS LQAHNKQQEK LLRTALGI
//